| IED ID | IndEnz0018000472 |
| Enzyme Type ID | peroxidase000472 |
| Protein Name |
Hydroxylamine reductase EC 1.7.99.1 Hybrid-cluster protein HCP Prismane protein |
| Gene Name | hcp ybjW b0873 JW0857 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIAALQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFDSPRIVGYAREAIALREALKAQCLAVDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATAGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIIDPTVGAYDDRIWTRSIVGWPGVRHLDGDDFSAVITQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA |
| Enzyme Length | 550 |
| Uniprot Accession Number | P75825 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by oxygen. Activated by cyanide except in the prolonged presence of excess cyanide, where the enzyme is inactivated. {ECO:0000269|PubMed:12374823}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine; Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938; EC=1.7.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:12374823}; |
| DNA Binding | |
| EC Number | 1.7.99.1 |
| Enzyme Function | FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:10651802, ECO:0000269|PubMed:12374823}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:12374823}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (12); Modified residue (1); Sequence conflict (1) |
| Keywords | 2Fe-2S;3D-structure;Cytoplasm;Iron;Iron-sulfur;Metal-binding;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: By Fnr, NarL and NarP under anaerobic conditions in the presence of either nitrate or nitrite. {ECO:0000269|PubMed:15667305}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}. |
| Modified Residue | MOD_RES 405; /note=Cysteine persulfide; /evidence=ECO:0000255|HAMAP-Rule:MF_00069 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 7DE4; |
| Mapped Pubmed ID | 15690043; 16606699; 24561554; 34101368; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,064 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for hydroxylamine (at pH 9) {ECO:0000269|PubMed:12374823}; Vmax=92 umol/min/mg enzyme (at pH 7.5) {ECO:0000269|PubMed:12374823}; Vmax=458 umol/min/mg enzyme (at pH 9) {ECO:0000269|PubMed:12374823}; |
| Metal Binding | METAL 3; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 6; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 18; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 25; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 249; /note=Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 273; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 317; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 405; /note=Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group; /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 433; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 458; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 492; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 494; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069 |
| Rhea ID | RHEA:22052 |
| Cross Reference Brenda |